scholarly journals Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth

2005 ◽  
Vol 169 (2) ◽  
pp. 341-354 ◽  
Author(s):  
Antonella Santuccione ◽  
Vladimir Sytnyk ◽  
Iryna Leshchyns'ka ◽  
Melitta Schachner

In spite of advances in understanding the role of the cellular prion protein (PrP) in neural cell interactions, the mechanisms of PrP function remain poorly characterized. We show that PrP interacts directly with the neural cell adhesion molecule (NCAM) and associates with NCAM at the neuronal cell surface. Both cis and trans interactions between NCAM at the neuronal surface and PrP promote recruitment of NCAM to lipid rafts and thereby regulate activation of fyn kinase, an enzyme involved in NCAM-mediated signaling. Cis and trans interactions between NCAM and PrP promote neurite outgrowth. When these interactions are disrupted in NCAM-deficient and PrP-deficient neurons or by PrP antibodies, NCAM/PrP-dependent neurite outgrowth is arrested, indicating that PrP is involved in nervous system development cooperating with NCAM as a signaling receptor.

2011 ◽  
Vol 21 (5) ◽  
pp. 1138-1144 ◽  
Author(s):  
W. Kudo ◽  
H.-P. Lee ◽  
W.-Q. Zou ◽  
X. Wang ◽  
G. Perry ◽  
...  

2001 ◽  
Vol 314 (5) ◽  
pp. 1209-1225 ◽  
Author(s):  
Gerold Schmitt-Ulms ◽  
Giuseppe Legname ◽  
Michael A Baldwin ◽  
Haydn L Ball ◽  
Nicole Bradon ◽  
...  

2010 ◽  
Vol 30 (27) ◽  
pp. 9292-9305 ◽  
Author(s):  
V. Devanathan ◽  
I. Jakovcevski ◽  
A. Santuccione ◽  
S. Li ◽  
H. J. Lee ◽  
...  

2006 ◽  
Vol 2006 ◽  
pp. 1-13 ◽  
Author(s):  
Mattia Toni ◽  
Enzo Spisni ◽  
Cristiana Griffoni ◽  
Spartaco Santi ◽  
Massimo Riccio ◽  
...  

It has been reported that cellular prion protein (PrPc) is enriched in caveolae or caveolae-like domains with caveolin-1 (Cav-1) participating to signal transduction events by Fyn kinase recruitment. By using the Glutathione-S-transferase (GST)-fusion proteins assay, we observed that PrPc strongly interacts in vitro with Cav-1. Thus, we ascertained the PrPc caveolar localization in a hypothalamic neuronal cell line (GN11), by confocal microscopy analysis, flotation on density gradient, and coimmunoprecipitation experiments. Following the anti-PrPc antibody-mediated stimulation of live GN11 cells, we observed that PrPc clustered on plasma membrane domains rich in Cav-1 in which Fyn kinase converged to be activated. After these events, a signaling cascade through p42/44 MAP kinase (Erk 1/2) was triggered, suggesting that following translocations from rafts to caveolae or caveolae-like domains PrPc could interact with Cav-1 and induce signal transduction events.


Author(s):  
Valeria Kaltezioti ◽  
Iosifina P. Foskolou ◽  
Matthieu D. Lavigne ◽  
Elpinickie Ninou ◽  
Matina Tsampoula ◽  
...  

2019 ◽  
Vol 112 (1) ◽  
pp. 1-21 ◽  
Author(s):  
Zuzana Fremuntova ◽  
Tibor Mosko ◽  
Jakub Soukup ◽  
Johanka Kucerova ◽  
Marie Kostelanska ◽  
...  

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